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The primary structure of protein L2 from the Escherichia coli ribosome
Author(s) -
Kimura Makoto,
Mende Liane,
Wittmann-Liebold Brigitte
Publication year - 1982
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(82)81122-8
Subject(s) - ribosome , protein primary structure , ribosomal protein , ribosomal rna , protein subunit , protein secondary structure , 50s , sequence (biology) , rna , escherichia coli , peptide sequence , biochemistry , chemistry , homologous chromosome , biology , gene
The complete primary structure of protein L2 which is the largest protein component of the E. coli 50 S subunit, has been established. A combination of enzymatic and chemical cleavages has been employed to isolate peptides, which were sequenced by the micro‐DABITC/PITC double‐coupling method [FEBS Lett. (1978) 93, 205–214]. The sequence determined shows protein L2 to consist of 272 amino acid residues with M r = 29730. Secondary structure predictions were made based on the primary structure. Further, sequence regions homologous to other ribosomal proteins are presented. These results suggest protein L2, which binds specifically to the 23 S RNA, to show homologous sequence stretches to the other RNA‐binding proteins.